In a biorefinery process, 5-Hydroxymethylfurfural (HMF) is a promising biomass-derived chemical with diverse industrial applications. The biotransformation of HMF to different high-valued furanic derivatives, such as 2,5-furandicarboxylic acid, 2,5-diformylfuran, 5-hydroxymethyl-2-furancarboxylic acid, and 5-formyl-2-furancarboxylic acid, has led to the transition from fossil-derived products to bio-based chemicals through sustainable routes. Although, chemocatalytic conversion of HMF has been extensively studied in the recent years, the higher selectivity, environment friendliness, and mild reaction conditions of HMF bioconversion has established these processes as a promising alternative to harsh chemical conditions. To understand the present status and challenges of HMF bioconversion, this review retrospects and describes the recent advancements in the biotransformation of HMF and systematically assesses the recent findings and developments in the HMF biotransformation through various reaction schemes. Further, this review illustrates, in comprehensive detail, the merits and challenges of various biological processes and it proposes a few research trends for economical and facile HMF bioconversion for commercialization.
In the present study, Candida antarctica lipase B was immobilized on amine‐functionalized silica microspheres as cross‐linked enzyme aggregates (CLEA) and utilized for the biomanufacturing of rhamnolipids (RL). Lipase CLEA synthesized under optimized conditions of 2.0:1.0 by volume of silica microsphere/enzyme concentration, a 1.0:2.5 (v/v) ratio of enzyme/2‐propanol, 7 mM glutaraldehyde concentration, when incubated at pH 9.0 and 40 °C, for a cross‐linking time of 30 min were observed to exhibit superior biocatalytic properties and a maximum enzyme load of 770 U g−1. Lipase CLEA exhibited enhanced pH stability in acidic and alkaline media and increased temperature resistance as compared to free lipase. Both free and CLEA lipases were used to synthesize RL in different solvent systems. After 12 h, from initiation of the esterification, the degree of esterification (molar conversion yield) reached 46% and 71% in the batch mode. 1H and 13C nuclear magnetic resonance (NMR) and high‐performance liquid chromatographic (HPLC) analysis confirm RL production by CLEA lipase. The CLEA showed greater confrontation to enzyme‐mediated bioprocess approach as compared to its soluble counterpart and exhibited excellent RL production and catalytic activity even after its tenth successive reuse.
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